Phosphorylation of the integrase protein of coliphage HK022

Mikhail Kolot, Rena Gorovits, Nava Silberstein, Boris Fichtman, Ezra Yagil*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The integrase (Int) proteins of coliphages HK022 and λ, are phosphorylated in one or more of their tyrosine residues. In Int of HK022 the phosphorylated residue(s) belong to its core-binding/catalytic domains. Wzc, a protein tyrosine kinase of Escherichia coli, is not required for Int phosphorylation in vivo, however, it can transphosphorylate the conserved Tyr342 catalytic residue of Int in vitro. Int purified from cells that overexpress Wzc has a reduced activity in vitro. In vivo, the lysogenization of wild type HK022 as well as of λ is not affected by the overexpression of Wzc. However, the nin5 mutant of λ, which lacks a protein-tyrosine phosphatase gene, shows a significantly reduced lysogenization. It is suggested that phosphorylation of Int by Wzc down regulates the activity of Int.

Original languageEnglish
Pages (from-to)383-390
Number of pages8
JournalVirology
Volume375
Issue number2
DOIs
StatePublished - 5 Jun 2008

Keywords

  • Integrase
  • Phage HK022
  • Protein phosphorylation
  • Wzc/Wzb

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